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Protein

Casein kinase II subunit alpha'

Gene

CSNK2A2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine. Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection. May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response. During mitosis, functions as a component of the p53/TP53-dependent spindle assembly checkpoint (SAC) that maintains cyclin-B-CDK1 activity and G2 arrest in response to spindle damage. Also required for p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53 following UV irradiation. Can also negatively regulate apoptosis. Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3. Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8. Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV. Also phosphorylates and regulates numerous transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, SRF, MAX, JUN, FOS, MYC and MYB. Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function. Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF1. Acts as an ectokinase that phosphorylates several extracellular proteins. During viral infection, phosphorylates various proteins involved in the viral life cycles of EBV, HSV, HBV, HCV, HIV, CMV and HPV.3 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Constitutively active protein kinase whose activity is not directly affected by phosphorylation. Seems to be regulated by level of expression and localization (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei69ATPPROSITE-ProRule annotation1
Active sitei157Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi46 – 54ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • protein N-terminus binding Source: UniProtKB
  • protein serine/threonine kinase activity Source: UniProtKB-KW

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • mitotic spindle checkpoint Source: UniProtKB
  • positive regulation of protein targeting to mitochondrion Source: ParkinsonsUK-UCL
  • protein folding Source: Reactome
  • regulation of mitophagy Source: ParkinsonsUK-UCL
  • regulation of signal transduction by p53 class mediator Source: Reactome
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • transcription, DNA-templated Source: UniProtKB-KW
  • Wnt signaling pathway Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Apoptosis, Cell cycle, Transcription, Transcription regulation, Wnt signaling pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:HS01010-MONOMER.
BRENDAi2.7.11.1. 2681.
ReactomeiR-HSA-1483191. Synthesis of PC.
R-HSA-201688. WNT mediated activation of DVL.
R-HSA-2514853. Condensation of Prometaphase Chromosomes.
R-HSA-445144. Signal transduction by L1.
R-HSA-6804756. Regulation of TP53 Activity through Phosphorylation.
R-HSA-6814122. Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
SignaLinkiP19784.
SIGNORiP19784.

Names & Taxonomyi

Protein namesi
Recommended name:
Casein kinase II subunit alpha' (EC:2.7.11.1)
Short name:
CK II alpha'
Gene namesi
Name:CSNK2A2
Synonyms:CK2A2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:2459. CSNK2A2.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

DisGeNETi1459.
OpenTargetsiENSG00000070770.
PharmGKBiPA26959.

Chemistry databases

ChEMBLiCHEMBL4070.
GuidetoPHARMACOLOGYi1550.

Polymorphism and mutation databases

BioMutaiCSNK2A2.
DMDMi125266.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000858911 – 350Casein kinase II subunit alpha'Add BLAST350

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei13PhosphotyrosineCombined sources1
Modified residuei18PhosphoserineCombined sources1
Modified residuei21PhosphoserineCombined sources1
Modified residuei97N6-acetyllysineCombined sources1
Modified residuei288PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP19784.
MaxQBiP19784.
PaxDbiP19784.
PeptideAtlasiP19784.
PRIDEiP19784.

2D gel databases

SWISS-2DPAGEP19784.

PTM databases

iPTMnetiP19784.
PhosphoSitePlusiP19784.

Expressioni

Gene expression databases

BgeeiENSG00000070770.
CleanExiHS_CSNK2A2.
ExpressionAtlasiP19784. baseline and differential.
GenevisibleiP19784. HS.

Interactioni

Subunit structurei

Heterotetramer composed of two catalytic subunits (alpha chain and/or alpha' chain) and two regulatory subunits (beta chains). The tetramer can exist as a combination of 2 alpha/2 beta, 2 alpha'/2 beta or 1 alpha/1 alpha'/2 beta subunits. Also part of a CK2-SPT16-SSRP1 complex composed of SSRP1, SUPT16H, CSNK2A1, CSNK2A2 and CSNK2B, which forms following UV irradiation. Interacts with RNPS1.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CSNK2A1P684006EBI-347451,EBI-347804
CSNK2BP678708EBI-347451,EBI-348169
KIF5CO602824EBI-347451,EBI-717170
TRIM41Q8WV445EBI-347451,EBI-725997

GO - Molecular functioni

  • protein N-terminus binding Source: UniProtKB

Protein-protein interaction databases

BioGridi107842. 212 interactors.
DIPiDIP-318N.
IntActiP19784. 151 interactors.
MINTiMINT-5004107.
STRINGi9606.ENSP00000262506.

Chemistry databases

BindingDBiP19784.

Structurei

Secondary structure

1350
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi11 – 13Combined sources3
Turni14 – 16Combined sources3
Helixi17 – 19Combined sources3
Helixi22 – 25Combined sources4
Helixi27 – 29Combined sources3
Helixi37 – 39Combined sources3
Beta strandi40 – 48Combined sources9
Beta strandi50 – 59Combined sources10
Turni60 – 63Combined sources4
Beta strandi64 – 71Combined sources8
Helixi76 – 88Combined sources13
Turni89 – 91Combined sources3
Beta strandi98 – 103Combined sources6
Turni105 – 107Combined sources3
Beta strandi110 – 115Combined sources6
Helixi122 – 125Combined sources4
Helixi131 – 150Combined sources20
Helixi160 – 162Combined sources3
Beta strandi163 – 166Combined sources4
Turni167 – 170Combined sources4
Beta strandi171 – 174Combined sources4
Helixi196 – 198Combined sources3
Helixi201 – 204Combined sources4
Helixi213 – 228Combined sources16
Beta strandi231 – 234Combined sources4
Helixi239 – 250Combined sources12
Helixi252 – 261Combined sources10
Helixi270 – 273Combined sources4
Helixi282 – 285Combined sources4
Turni288 – 290Combined sources3
Helixi291 – 293Combined sources3
Helixi296 – 305Combined sources10
Turni310 – 312Combined sources3
Helixi316 – 320Combined sources5
Helixi323 – 325Combined sources3
Helixi326 – 331Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3E3BX-ray3.20X1-334[»]
3OFMX-ray2.00A1-350[»]
3U87X-ray2.90A/B327-350[»]
ProteinModelPortaliP19784.
SMRiP19784.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19784.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini40 – 325Protein kinasePROSITE-ProRule annotationAdd BLAST286

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CK2 subfamily.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0668. Eukaryota.
ENOG410XNPP. LUCA.
GeneTreeiENSGT00390000004215.
HOGENOMiHOG000233021.
HOVERGENiHBG107282.
KOiK03097.
OMAiNREYWDY.
OrthoDBiEOG091G0AZY.
PhylomeDBiP19784.
TreeFamiTF300483.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P19784-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPGPAAGSRA RVYAEVNSLR SREYWDYEAH VPSWGNQDDY QLVRKLGRGK
60 70 80 90 100
YSEVFEAINI TNNERVVVKI LKPVKKKKIK REVKILENLR GGTNIIKLID
110 120 130 140 150
TVKDPVSKTP ALVFEYINNT DFKQLYQILT DFDIRFYMYE LLKALDYCHS
160 170 180 190 200
KGIMHRDVKP HNVMIDHQQK KLRLIDWGLA EFYHPAQEYN VRVASRYFKG
210 220 230 240 250
PELLVDYQMY DYSLDMWSLG CMLASMIFRR EPFFHGQDNY DQLVRIAKVL
260 270 280 290 300
GTEELYGYLK KYHIDLDPHF NDILGQHSRK RWENFIHSEN RHLVSPEALD
310 320 330 340 350
LLDKLLRYDH QQRLTAKEAM EHPYFYPVVK EQSQPCADNA VLSSGLTAAR
Length:350
Mass (Da):41,213
Last modified:February 1, 1991 - v1
Checksum:i3ECB92F6BD3DD7F1
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_040416188E → A.1 PublicationCorresponds to variant rs55911801dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55268 mRNA. Translation: AAA51548.1.
BC008812 mRNA. Translation: AAH08812.1.
CCDSiCCDS10794.1.
PIRiB35838.
RefSeqiNP_001887.1. NM_001896.2.
UniGeneiHs.82201.

Genome annotation databases

EnsembliENST00000262506; ENSP00000262506; ENSG00000070770.
GeneIDi1459.
KEGGihsa:1459.
UCSCiuc002enc.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55268 mRNA. Translation: AAA51548.1.
BC008812 mRNA. Translation: AAH08812.1.
CCDSiCCDS10794.1.
PIRiB35838.
RefSeqiNP_001887.1. NM_001896.2.
UniGeneiHs.82201.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3E3BX-ray3.20X1-334[»]
3OFMX-ray2.00A1-350[»]
3U87X-ray2.90A/B327-350[»]
ProteinModelPortaliP19784.
SMRiP19784.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107842. 212 interactors.
DIPiDIP-318N.
IntActiP19784. 151 interactors.
MINTiMINT-5004107.
STRINGi9606.ENSP00000262506.

Chemistry databases

BindingDBiP19784.
ChEMBLiCHEMBL4070.
GuidetoPHARMACOLOGYi1550.

PTM databases

iPTMnetiP19784.
PhosphoSitePlusiP19784.

Polymorphism and mutation databases

BioMutaiCSNK2A2.
DMDMi125266.

2D gel databases

SWISS-2DPAGEP19784.

Proteomic databases

EPDiP19784.
MaxQBiP19784.
PaxDbiP19784.
PeptideAtlasiP19784.
PRIDEiP19784.

Protocols and materials databases

DNASUi1459.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262506; ENSP00000262506; ENSG00000070770.
GeneIDi1459.
KEGGihsa:1459.
UCSCiuc002enc.4. human.

Organism-specific databases

CTDi1459.
DisGeNETi1459.
GeneCardsiCSNK2A2.
HGNCiHGNC:2459. CSNK2A2.
MIMi115442. gene.
neXtProtiNX_P19784.
OpenTargetsiENSG00000070770.
PharmGKBiPA26959.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0668. Eukaryota.
ENOG410XNPP. LUCA.
GeneTreeiENSGT00390000004215.
HOGENOMiHOG000233021.
HOVERGENiHBG107282.
KOiK03097.
OMAiNREYWDY.
OrthoDBiEOG091G0AZY.
PhylomeDBiP19784.
TreeFamiTF300483.

Enzyme and pathway databases

BioCyciZFISH:HS01010-MONOMER.
BRENDAi2.7.11.1. 2681.
ReactomeiR-HSA-1483191. Synthesis of PC.
R-HSA-201688. WNT mediated activation of DVL.
R-HSA-2514853. Condensation of Prometaphase Chromosomes.
R-HSA-445144. Signal transduction by L1.
R-HSA-6804756. Regulation of TP53 Activity through Phosphorylation.
R-HSA-6814122. Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
SignaLinkiP19784.
SIGNORiP19784.

Miscellaneous databases

ChiTaRSiCSNK2A2. human.
EvolutionaryTraceiP19784.
GeneWikiiCSNK2A2.
GenomeRNAii1459.
PROiP19784.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000070770.
CleanExiHS_CSNK2A2.
ExpressionAtlasiP19784. baseline and differential.
GenevisibleiP19784. HS.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCSK22_HUMAN
AccessioniPrimary (citable) accession number: P19784
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: November 30, 2016
This is version 180 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

Can use both ATP and GTP as phosphoryl donors. Phosphorylation by casein kinase 2 has been estimated to represent up to one quarter of the eukaryotic phosphoproteome.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.